ライフサイエンスコーパス: ATP sulfurylase

1 ional ("PAPS synthetase") ancestor of fungal ATP sulfurylase.

2 C-terminal domain that is present in fungal ATP sulfurylase.

3 progress curves during the first turnover of ATP sulfurylase.

4 netic differences between the two classes of ATP sulfurylase.

5 NH2-terminal APS kinase and a COOH-terminal ATP sulfurylase.

6 6 encode APS kinase, while exons 6-13 encode ATP sulfurylase.

7 target superoxide dismutases, laccases, and ATP sulfurylases.

8 ATP and a carrier-free [35S]-Na2(35)SO4 with ATP sulfurylase, a recombinant APS kinase and inorganic

9 Comparison of the Aquifex ATP sulfurylase active site with those from sulfate assi

10 By contrast, total ATP sulfurylase activity declines proportionally in all

11 mportant role for the HXGH histidines in the ATP sulfurylase activity of bifunctional PAPS synthase a

12 ulfate as the sole sulfur source and exhibit ATP sulfurylase activity.

13 activity, whereas a 220-623 fragment evinced ATP sulfurylase activity.

14 ne ablated APS kinase activity while leaving ATP-sulfurylase activity intact.

15 G59A caused a significant decrease in ATP-sulfurylase activity without effect on APS kinase ac

16 Mammalian ATP sulfurylase/adenosine 5'-phosphosulfate (APS) kinase

17 lase domain of the mouse bifunctional enzyme ATP sulfurylase/adenosine 5'-phosphosulfate (APS) kinase

18 The recently cloned murine ATP-sulfurylase/adenosine 5'-phosphosulfate (APS) kinase

19 ATP sulfurylase and 5'-adenylylsulfate (APS) reductase c

20 ), is synthesized by the concerted action of ATP sulfurylase and adenosine 5'-phosphosulfate (APS) ki

21 expresses a gene product that exhibits both ATP sulfurylase and adenosine-5'-phosphosulfate (APS) ki

22 The (a) imbalance between ATP sulfurylase and APS kinase activities, (b) accumulat

23 In simpler organisms, the ATP sulfurylase and APS kinase reactions are catalyzed b

24 quential actions of two cytoplasmic enzymes, ATP sulfurylase and APS kinase, and then must be transfe

25 t into the nature and control of the enzymes ATP sulfurylase and APS kinase, which catalyze the early

26 of Arabidopsis plants the total activity of ATP sulfurylase and APS reductase declines by 3-fold in

27 e chemiluminescent detection of PP(i), using ATP sulfurylase and firefly luciferase, was adapted to m

28 p composed of cysteine biosynthesis enzymes, ATP sulfurylase and O-acetylserine sulfhydrylase, each w

29 ubunit containing an adenosine triphosphate (ATP) sulfurylase and an adenosine 5'-phosphosulfate (APS

30 furylase kinase (SK) polypeptide having both ATP-sulfurylase and adenosine-phosphosulfate kinase acti

31 ATP-sulfurylase and APS-kinase can rapidly synthesize ad

32 ctivity of the two enzymes of its synthesis, ATP-sulfurylase and APS-kinase.

33 e of selenate, (b) activation of selenate by ATP sulfurylase, and (b) conversion of selenomethionine

34 of functions of this unique protein (reverse ATP-sulfurylase, APS kinase, and an overall assay) were

35 esolution X-ray crystal structure of Aquifex ATP sulfurylase-APS kinase bifunctional enzyme is presen

36 ches and sequence comparison of bifunctional ATP sulfurylase/APS kinase and monofunctional ATP sulfur

37 ATP sulfurylase/APS kinase catalyses the metabolic activ

38 ous genes, ATPSK2 and Atpsk2, encoding novel ATP sulfurylase/APS kinase orthologues in the respective

39 finity sulfate transporter (AST68) and three ATP sulfurylases (APS1, APS3 and APS4) in higher plants.

40 Reduced expression of ATP sulfurylase (ATPS) alone affects both sulfate transl

41 d the activity of key S assimilatory enzymes ATP sulfurylase (ATPS), APS reductase (APR), and serine

42 of sulfate through adenylation by the enzyme ATP sulfurylase (ATPS), forming adenosine 5'-phosphosulf

43 high-affinity sulphate transporter and three ATP sulfurylases (ATPS) were the target genes of AthmiR3

44 t dimerization interface compared with other ATP sulfurylases but was similar to mammalian 3'-phospho

45 The distinct behavior of ATP sulfurylase can be attributed to reciprocal expressi

46 ATP sulfurylase catalyzes and couples the free energies

47 sulfur-assimilating organisms such as fungi, ATP sulfurylase catalyzes the first committed step in su

48 ydomonas reinhardtii adenosine triphosphate (ATP) sulfurylase cDNA clone (pATS1) was selected by comp

49 he amino acid sequence of the C. reinhardtii ATP sulfurylase, derived from the nucleotide sequence of

50 APS kinase-like C-terminal region of fungal ATP sulfurylase does not account for the lack of APS kin

51 amma phosphodiester bond of ATP, whereas the ATP sulfurylase domain involves cleavage of the alpha-be

52 elected mutagenesis of the HXGH motif in the ATP sulfurylase domain of human PAPS synthase (amino aci

53 the highly conserved HXGH motif found in the ATP sulfurylase domain of PAPS synthases is involved in

54 ence of a highly conserved HXGH motif in the ATP sulfurylase domain of PAPS synthases, a motif implic

55 The kinetic constants of the ATP sulfurylase domain were as follows: V(max,f) = 0.77

56 state, chlorate, and perchlorate bind to the ATP sulfurylase domain, with the first five serving as a

57 Expressed protein generated from the ATP-sulfurylase domain alone was fully active in both th

58 The former reaction is catalyzed by the ATP-sulfurylase domain and the latter by the APS-kinase

59 PAPS) synthetase consists of a COOH-terminal ATP-sulfurylase domain covalently linked through a nonho

60 Because the ATP-sulfurylase domain of PAPS synthetase influences the

61 second step in which APS, the product of the ATP-sulfurylase domain, is phosphorylated on its 3'-hydr

62 ATP sulfurylase domains are often embedded in multifunct

63 herichia coli cysDN genes, which code for an ATP sulfurylase (EC 2.7.7.4).

64 in the analogous C-terminal region of fungal ATP sulfurylase eliminated enzyme activity.

65 ATP sulfurylase from Penicillium chrysogenum is a homohe

66 ATP sulfurylase from Penicillium chrysogenum is an allos

67 ATP sulfurylase from Penicillium chrysogenum is an allos

68 We present here, the crystal structure of ATP sulfurylase from this bacterium at 1.7 A resolution.

69 ATP sulfurylase, from E. coli Kappa-12, is a GTPase.targ

70 ATP sulfurylase, from Escherichia coli K-12, catalyzes a

71 ATP sulfurylase, from Escherichia coli K-12, conformatio

72 ATP sulfurylase, from Escherichia coli Kappa-12, is a GT

73 ulfur chemolithotrophic bacteria, the enzyme ATP sulfurylase functions to produce ATP and inorganic s

74 selected by complementing a mutation in the ATP sulfurylase gene (cysD) of Escherichia coli.

75 roduct release step(s) were confirmed in the ATP sulfurylase-GTPase reaction by a burst of product in

76 -bond cleavage in the catalytic cycle of the ATP sulfurylase-GTPase, from E. coli K-12.

77 In contrast, ATP sulfurylase in sulfur chemolithotrophs catalyzes the

78 ne (ATS1), is 25 to 40% identical to that of ATP sulfurylases in other eukaryotic organisms and has a

79 furylase isoform 1 from soybean (Glycine max ATP sulfurylase) in complex with APS was determined.

80 lled by the binding of activators that drive ATP sulfurylase into forms that mimic different stages o

81 The mechanism of ATP sulfurylase involves an enzyme isomerization that pr

82 nding of mGMPPNP to the E.AMP.PPi complex of ATP sulfurylase is biphasic, indicating that an isomeriz

83 ionation of Arabidopsis leaves revealed that ATP sulfurylase isoenzymes exist in the chloroplast and

84 ble reaction, the x-ray crystal structure of ATP sulfurylase isoform 1 from soybean (Glycine max ATP

85 ATP sulfurylase, isolated from Escherichia coli K-12, ca

86 ATP sulfurylase, isolated from Escherichia coli K-12, is

87 ontrast to the wild type enzyme, recombinant ATP sulfurylase lacking the C-terminal allosteric domain

88 e bifunctional enzyme, from which the fungal ATP sulfurylase may have evolved.

89 ATP sulfurylase mRNA was present when cells were grown i

90 Disruption of met3 or met14 genes (ATP sulfurylase or phosphosulfate kinase), transcription

91 structure and kinetic analysis suggest that ATP sulfurylase overcomes the energetic barrier of APS s

92 In total, the results suggest that cytosolic ATP sulfurylase plays a specialized function that is pro

93 Steady-state kinetic analysis of 20 G. max ATP sulfurylase point mutants suggests a reaction mechan

94 reactions in the sulfate activation pathway, ATP-sulfurylase (S) and APS-kinase (K), are fused as 'KS

95 TP sulfurylase/APS kinase and monofunctional ATP sulfurylases shows a limited number of highly conser

96 nd the mechanism of energetic linkage in the ATP sulfurylase system are discussed.

97 acterium was found to contain high levels of ATP sulfurylase that may provide a substantial fraction

98 tically linked to the chemistry catalyzed by ATP sulfurylase, the first enzyme in the cysteine biosyn

99 which targets three out of four isoforms of ATP sulfurylase, the first enzyme of sulfate assimilatio

100 nscription factor maintain optimal levels of ATP sulfurylase transcripts to enable increased flux thr

101 ed wild-type plants and in selenate-supplied ATP-sulfurylase transgenic plants.

102 lanine, reported to be an inhibitor of brain ATP sulfurylase, was without effect on PAPS synthetase i

103 teady-state stages of the catalytic cycle of ATP sulfurylase were studied using tools capable of dist

104 Aquifex enzyme is reminiscent of the fungal ATP sulfurylase, which contains a C-terminal domain that

105 QTL encodes the ATPS1 isoform of the enzyme ATP sulfurylase, which precedes adenosine 5'-phosphosulf

106 mmitted step in this pathway is catalyzed by ATP sulfurylase, which synthesizes adenosine 5'-phosphos

107 Consequently, ATP sulfurylases, which catalyze APS synthesis, suffer a

108 in the reported crystal structures of fungal ATP sulfurylases, which contained bound substrates, but

109 The expressed monofunctional ATP-sulfurylase, which was initially fully active, was u